Q8WXH0 (SYNE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 122.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nesprin-2 Alternative name(s): Nuclear envelope spectrin repeat protein 2 Nucleus and actin connecting element protein Short name=Protein NUANCE Synaptic nuclear envelope protein 2 Short name=Syne-2 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 6885 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for centrosome migration to the apical cell surface during early ciliogenesis. Ref.1 Ref.14 Ref.16 Ref.21 |
| Subunit structure | Component of LINC complexes composed of SUN domain-containing proteins SUN1 or SUN2 coupled to KASH domain-containing proteins (SYNE1, SYNE2 or SYNE3), also called nesprins. Interacts with F-actin via its N-terminal domain. Interacts with EMD, LMNA and MKS3. Ref.1 Ref.13 Ref.14 Ref.16 Ref.19 |
| Subcellular location | Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Potential. Sarcoplasmic reticulum membrane; Single-pass type IV membrane protein Potential. Cell membrane; Single-pass membrane protein Potential. Cytoplasm › cytoskeleton. Mitochondrion. Nucleus › nucleoplasm. Note: Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter solubles isoforms can be found in the cytoplasm and within the nucleus. Ref.12 Ref.13 Ref.16 |
| Tissue specificity | Widely expressed, with higher level in kidney, adult and fetal liver, stomach and placenta. Weakly expressed in skeletal muscle and brain. Isoform 5 is highly expressed in pancreas, skeletal muscle and heart. Ref.13 |
| Domain | The KASH domain mediates the nuclear envelope targeting. Ref.14 |
| Involvement in disease | Emery-Dreifuss muscular dystrophy 5 (EDMD5) [MIM:612999]: A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. |
| Sequence similarities | Belongs to the nesprin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 1 KASH domain. Contains 9 spectrin repeats. |
| Sequence caution | The sequence BAB84881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAB45729.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB55905.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| APPL1 | Q9UKG1 | 3 | EBI-2372294,EBI-741243 | |
| SUN1 | O94901 | 2 | EBI-6170976,EBI-2796904 | |
| SUN2 | Q9UH99 | 5 | EBI-2372294,EBI-1044964 |
Alternative products
| This entry describes 9 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8WXH0-1) Also known as: Nesprin-2 Giant; NUANCE; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q8WXH0-2) The sequence of this isoform differs from the canonical sequence as follows: 6444-6444: S → SDVEIPENPEAYLKMTTKTLKASS 6801-6801: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q8WXH0-3) The sequence of this isoform differs from the canonical sequence as follows: 1-6030: Missing. | ||||||
| Note: Produced by exon skipping that results in a frameshift. No experimental confirmation available. | ||||||
| Isoform 4 (identifier: Q8WXH0-4) Also known as: Beta; The sequence of this isoform differs from the canonical sequence as follows: 1-6122: Missing. | ||||||
| Isoform 5 (identifier: Q8WXH0-5) Also known as: Alpha; The sequence of this isoform differs from the canonical sequence as follows: 1-6366: Missing. 6444-6444: S → SDVEIPENPEAYLKMTTKTLKASS 6664-6664: Q → QGSKTRPRSDVLFFK | ||||||
| Isoform 6 (identifier: Q8WXH0-6) The sequence of this isoform differs from the canonical sequence as follows: 1-6469: Missing. 6664-6664: Q → QGSKTRPRSDVLFFK 6801-6801: Missing. | ||||||
| Isoform 7 (identifier: Q8WXH0-7) Also known as: Gamma; The sequence of this isoform differs from the canonical sequence as follows: 1-3638: Missing. 3828-3828: Q → QDSKCFRSGPRPNIYVSYYVTVIQ | ||||||
| Isoform 8 (identifier: Q8WXH0-8) The sequence of this isoform differs from the canonical sequence as follows: 263-285: DVDVVDPDEKSIMTYVAQFLQYS → DAWRSSALYRIYMPGTVSCASYL 286-6885: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 9 (identifier: Q8WXH0-9) Also known as: NUANCE-N-33; The sequence of this isoform differs from the canonical sequence as follows: 263-267: DVDVV → AYKNF 268-6885: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||
Molecule processing | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 6885 | 6885 | Nesprin-2 | PRO_0000163592 | ||||||||||
Regions | ||||||||||||||
| Topological domain | 1 – 6834 | 6834 | Cytoplasmic Potential | |||||||||||
| Transmembrane | 6835 – 6855 | 21 | Helical; Anchor for type IV membrane protein; Potential | |||||||||||
| Topological domain | 6856 – 6885 | 30 | Perinuclear space Potential | |||||||||||
| Domain | 1 – 286 | 286 | Actin-binding | |||||||||||
| Domain | 31 – 136 | 106 | CH 1 | |||||||||||
| Domain | 181 – 286 | 106 | CH 2 | |||||||||||
| Repeat | 4944 – 5053 | 110 | Spectrin 1 | |||||||||||
| Repeat | 5054 – 5167 | 114 | Spectrin 2 | |||||||||||
| Repeat | 5170 – 5274 | 105 | Spectrin 3 | |||||||||||
| Repeat | 5852 – 5914 | 63 | Spectrin 4 | |||||||||||
| Repeat | 5917 – 6019 | 103 | Spectrin 5 | |||||||||||
| Repeat | 6022 – 6133 | 112 | Spectrin 6 | |||||||||||
| Repeat | 6136 – 6242 | 107 | Spectrin 7 | |||||||||||
| Repeat | 6245 – 6349 | 105 | Spectrin 8 | |||||||||||
| Repeat | 6551 – 6658 | 108 | Spectrin 9 | |||||||||||
| Domain | 6826 – 6885 | 60 | KASH | |||||||||||
| Coiled coil | 233 – 255 | 23 | Potential | |||||||||||
| Coiled coil | 306 – 323 | 18 | Potential | |||||||||||
| Coiled coil | 461 – 477 | 17 | Potential | |||||||||||
| Coiled coil | 810 – 909 | 100 | Potential | |||||||||||
| Coiled coil | 941 – 972 | 32 | Potential | |||||||||||
| Coiled coil | 1008 – 1041 | 34 | Potential | |||||||||||
| Coiled coil | 1194 – 1222 | 29 | Potential | |||||||||||
| Coiled coil | 1299 – 1332 | 34 | Potential | |||||||||||
| Coiled coil | 1462 – 1494 | 33 | Potential | |||||||||||
| Coiled coil | 1566 – 1602 | 37 | Potential | |||||||||||
| Coiled coil | 1658 – 1708 | 51 | Potential | |||||||||||
| Coiled coil | 1747 – 1771 | 25 | Potential | |||||||||||
| Coiled coil | 1782 – 1804 | 23 | Potential | |||||||||||
| Coiled coil | 1923 – 1965 | 43 | Potential | |||||||||||
| Coiled coil | 2007 – 2035 | 29 | Potential | |||||||||||
| Coiled coil | 2176 – 2205 | 30 | Potential | |||||||||||
| Coiled coil | 2282 – 2369 | 88 | Potential | |||||||||||
| Coiled coil | 2422 – 2478 | 57 | Potential | |||||||||||
| Coiled coil | 2589 – 2650 | 62 | Potential | |||||||||||
| Coiled coil | 2696 – 2717 | 22 | Potential | |||||||||||
| Coiled coil | 2802 – 2835 | 34 | Potential | |||||||||||
| Coiled coil | 2866 – 2975 | 110 | Potential | |||||||||||
| Coiled coil | 3014 – 3057 | 44 | Potential | |||||||||||
| Coiled coil | 3087 – 3132 | 46 | Potential | |||||||||||
| Coiled coil | 3207 – 3241 | 35 | Potential | |||||||||||
| Coiled coil | 3297 – 3428 | 132 | Potential | |||||||||||
| Coiled coil | 3464 – 3505 | 42 | Potential | |||||||||||
| Coiled coil | 3553 – 3584 | 32 | Potential | |||||||||||
| Coiled coil | 3655 – 3723 | 69 | Potential | |||||||||||
| Coiled coil | 3778 – 3799 | 22 | Potential | |||||||||||
| Coiled coil | 3853 – 3911 | 59 | Potential | |||||||||||
| Coiled coil | 3971 – 4069 | 99 | Potential | |||||||||||
| Coiled coil | 4272 – 4299 | 28 | Potential | |||||||||||
| Coiled coil | 4307 – 4339 | 33 | Potential | |||||||||||
| Coiled coil | 4493 – 4536 | 44 | Potential | |||||||||||
| Coiled coil | 4636 – 4701 | 66 | Potential | |||||||||||
| Coiled coil | 4831 – 4861 | 31 | Potential | |||||||||||
| Coiled coil | 4911 – 4944 | 34 | Potential | |||||||||||
| Coiled coil | 5308 – 5346 | 39 | Potential | |||||||||||
| Coiled coil | 5428 – 5445 | 18 | Potential | |||||||||||
| Coiled coil | 5505 – 5529 | 25 | Potential | |||||||||||
| Coiled coil | 6697 – 6770 | 74 | Potential | |||||||||||
Amino acid modifications | ||||||||||||||
| Modified residue | 955 | 1 | N6-acetyllysine Ref.18 | |||||||||||
| Modified residue | 2781 | 1 | Phosphoserine Ref.20 Ref.23 | |||||||||||
| Modified residue | 4108 | 1 | Phosphoserine Ref.15 Ref.17 | |||||||||||
| Modified residue | 6361 | 1 | Phosphoserine Ref.20 | |||||||||||
Natural variations | ||||||||||||||
| Alternative sequence | 1 – 6469 | 6469 | Missing in isoform 6. | VSP_007158 | ||||||||||
| Alternative sequence | 1 – 6366 | 6366 | Missing in isoform 5. | VSP_007157 | ||||||||||
| Alternative sequence | 1 – 6122 | 6122 | Missing in isoform 4. | VSP_007156 | ||||||||||
| Alternative sequence | 1 – 6030 | 6030 | Missing in isoform 3. | VSP_007155 | ||||||||||
| Alternative sequence | 1 – 3638 | 3638 | Missing in isoform 7. | VSP_007154 | ||||||||||
| Alternative sequence | 263 – 285 | 23 | DVDVV…FLQYS → DAWRSSALYRIYMPGTVSCA SYL in isoform 8. | VSP_007161 | ||||||||||
| Alternative sequence | 263 – 267 | 5 | DVDVV → AYKNF in isoform 9. | VSP_007159 | ||||||||||
| Alternative sequence | 268 – 6885 | 6618 | Missing in isoform 9. | VSP_007160 | ||||||||||
| Alternative sequence | 286 – 6885 | 6600 | Missing in isoform 8. | VSP_007162 | ||||||||||
| Alternative sequence | 3828 | 1 | Q → QDSKCFRSGPRPNIYVSYYV TVIQ in isoform 7. | VSP_007163 | ||||||||||
| Alternative sequence | 6444 | 1 | S → SDVEIPENPEAYLKMTTKTL KASS in isoform 2 and isoform 5. | VSP_007164 | ||||||||||
| Alternative sequence | 6664 | 1 | Q → QGSKTRPRSDVLFFK in isoform 5 and isoform 6. | VSP_007165 | ||||||||||
| Alternative sequence | 6801 | 1 | Missing in isoform 2 and isoform 6. | VSP_007166 | ||||||||||
| Natural variant | 8 | 1 | P → S. Corresponds to variant rs2275017 [ dbSNP | Ensembl ]. | VAR_027947 | ||||||||||
| Natural variant | 432 | 1 | S → R. Corresponds to variant rs35554503 [ dbSNP | Ensembl ]. | VAR_050238 | ||||||||||
| Natural variant | 574 | 1 | I → T. Corresponds to variant rs9944035 [ dbSNP | Ensembl ]. | VAR_027948 | ||||||||||
| Natural variant | 1393 | 1 | R → W. Corresponds to variant rs17751301 [ dbSNP | Ensembl ]. | VAR_050239 | ||||||||||
| Natural variant | 1969 | 1 | M → T. Ref.1 Corresponds to variant rs4902264 [ dbSNP | Ensembl ]. | VAR_050240 | ||||||||||
| Natural variant | 2284 | 1 | A → V. Ref.1 Corresponds to variant rs4027402 [ dbSNP | Ensembl ]. | VAR_050241 | ||||||||||
| Natural variant | 2347 | 1 | A → E. Corresponds to variant rs34625768 [ dbSNP | Ensembl ]. | VAR_050242 | ||||||||||
| Natural variant | 2358 | 1 | N → S. Corresponds to variant rs4027404 [ dbSNP | Ensembl ]. | VAR_027949 | ||||||||||
| Natural variant | 2359 | 1 | S → G. Corresponds to variant rs7157465 [ dbSNP | Ensembl ]. | VAR_050243 | ||||||||||
| Natural variant | 2359 | 1 | S → N. Ref.1 Corresponds to variant rs4027404 [ dbSNP | Ensembl ]. | VAR_050244 | ||||||||||
| Natural variant | 2394 | 1 | A → T. Corresponds to variant rs4027405 [ dbSNP | Ensembl ]. | VAR_027950 | ||||||||||
| Natural variant | 2395 | 1 | A → T. Ref.1 Corresponds to variant rs4027405 [ dbSNP | Ensembl ]. | VAR_050245 | ||||||||||
| Natural variant | 2490 | 1 | V → G. Corresponds to variant rs34393543 [ dbSNP | Ensembl ]. | VAR_050246 | ||||||||||
| Natural variant | 2564 | 1 | I → V. Corresponds to variant rs11628107 [ dbSNP | Ensembl ]. | VAR_050247 | ||||||||||
| Natural variant | 2801 | 1 | G → S. Corresponds to variant rs1890908 [ dbSNP | Ensembl ]. | VAR_027951 | ||||||||||
| Natural variant | 2802 | 1 | S → G. Ref.1 Corresponds to variant rs1890908 [ dbSNP | Ensembl ]. | VAR_050248 | ||||||||||
| Natural variant | 2942 | 1 | I → V. Ref.1 Corresponds to variant rs3829767 [ dbSNP | Ensembl ]. | VAR_050249 | ||||||||||
| Natural variant | 3026 | 1 | E → D. Corresponds to variant rs34843668 [ dbSNP | Ensembl ]. | VAR_050250 | ||||||||||
| Natural variant | 3130 | 1 | N → S. Corresponds to variant rs11847087 [ dbSNP | Ensembl ]. | VAR_050251 | ||||||||||
| Natural variant | 3253 | 1 | D → H. Ref.1 Corresponds to variant rs8010911 [ dbSNP | Ensembl ]. | VAR_050252 | ||||||||||
| Natural variant | 3309 | 1 | H → R. Ref.1 Corresponds to variant rs8010699 [ dbSNP | Ensembl ]. | VAR_050253 | ||||||||||
| Natural variant | 3523 | 1 | K → Q. Corresponds to variant rs35203186 [ dbSNP | Ensembl ]. | VAR_050254 | ||||||||||
| Natural variant | 3982 | 1 | N → H. Corresponds to variant rs10137972 [ dbSNP | Ensembl ]. | VAR_050255 | ||||||||||
| Natural variant | 4041 | 1 | R → H. Corresponds to variant rs17101661 [ dbSNP | Ensembl ]. | VAR_050256 | ||||||||||
| Natural variant | 4912 | 1 | P → A. Corresponds to variant rs17766354 [ dbSNP | Ensembl ]. | VAR_050257 | ||||||||||
| Natural variant | 4913 | 1 | E → K. Corresponds to variant rs12881815 [ dbSNP | Ensembl ]. | VAR_050258 | ||||||||||
| Natural variant | 5086 | 1 | H → Y. Corresponds to variant rs2039475 [ dbSNP | Ensembl ]. | VAR_050259 | ||||||||||
| Natural variant | 5186 | 1 | L → M. Ref.1 Ref.7 Corresponds to variant rs10151658 [ dbSNP | Ensembl ]. | VAR_050260 | ||||||||||
| Natural variant | 5547 | 1 | D → N. Corresponds to variant rs17179194 [ dbSNP | Ensembl ]. | VAR_050261 | ||||||||||
| Natural variant | 5940 | 1 | V → I in a breast cancer sample; somatic mutation. Ref.24 | VAR_036255 | ||||||||||
| Natural variant | 6155 | 1 | A → V. Corresponds to variant rs2275014 [ dbSNP | Ensembl ]. | VAR_050262 | ||||||||||
| Natural variant | 6200 | 1 | Y → C in a breast cancer sample; somatic mutation. Ref.24 | VAR_036256 | ||||||||||
| Natural variant | 6211 | 1 | T → M in EDMD5. Ref.25 | VAR_062977 | ||||||||||
| Natural variant | 6681 | 1 | K → E. Corresponds to variant rs35315070 [ dbSNP | Ensembl ]. | VAR_050263 | ||||||||||
| Natural variant | 6697 | 1 | R → W. Corresponds to variant rs35700578 [ dbSNP | Ensembl ]. | VAR_050264 | ||||||||||
Experimental info | ||||||||||||||
| Sequence conflict | 668 | 1 | Missing Ref.3 | |||||||||||
| Sequence conflict | 1087 | 1 | M → T Ref.3 | |||||||||||
| Sequence conflict | 3115 | 1 | F → S in AAL33548. Ref.1 | |||||||||||
| Sequence conflict | 3193 | 1 | E → G in AAL33548. Ref.1 | |||||||||||
| Sequence conflict | 3951 | 1 | Q → L in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4001 | 1 | W → Q in AAN60443. Ref.3 | |||||||||||
| Sequence conflict | 4158 | 1 | S → F in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4158 | 1 | S → F Ref.3 | |||||||||||
| Sequence conflict | 4209 | 1 | I → T in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4209 | 1 | I → T Ref.3 | |||||||||||
| Sequence conflict | 4327 | 1 | E → Q in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4327 | 1 | E → Q Ref.3 | |||||||||||
| Sequence conflict | 4418 | 1 | N → K in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4418 | 1 | N → K Ref.3 | |||||||||||
| Sequence conflict | 4713 | 1 | E → G in AAL33548. Ref.1 | |||||||||||
| Sequence conflict | 4733 | 1 | P → S in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4733 | 1 | P → S Ref.3 | |||||||||||
| Sequence conflict | 4807 | 1 | N → I in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4807 | 1 | N → I Ref.3 | |||||||||||
| Sequence conflict | 4826 | 1 | S → P in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 4826 | 1 | S → P Ref.3 | |||||||||||
| Sequence conflict | 5166 | 1 | E → D in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 5166 | 1 | E → D Ref.3 | |||||||||||
| Sequence conflict | 5646 | 1 | T → A in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 5646 | 1 | T → A Ref.3 | |||||||||||
| Sequence conflict | 5727 | 1 | K → R in AAL33802. Ref.2 | |||||||||||
| Sequence conflict | 5727 | 1 | K → R Ref.3 | |||||||||||
Secondary structure | ||||||||||||||
Helix Strand Turn | ||||||||||||||
| Turn | 6867 – 6870 | 4 | ||||||||||||
| Beta strand | 6871 – 6873 | 3 | ||||||||||||
| Beta strand | 6875 – 6881 | 7 | ||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "NUANCE, a giant protein connecting the nucleus and actin cytoskeleton." Zhen Y.-Y., Libotte T., Munck M., Noegel A.A., Korenbaum E. J. Cell Sci. 115:3207-3222(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 9), FUNCTION, CHARACTERIZATION, INTERACTION WITH F-ACTIN, VARIANTS THR-1969; VAL-2284; ASN-2359; THR-2395; GLY-2802; VAL-2942; HIS-3253; ARG-3309 AND MET-5186. |
| [2] | "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues." Zhang Q., Skepper J.N., Yang F., Davies J.D., Hegyi L., Roberts R.G., Weissberg P.L., Ellis J.A., Shanahan C.M. J. Cell Sci. 114:4485-4498(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7). |
| [3] | "The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300." Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G. Genomics 80:473-481(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [4] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Testis. |
| [5] | "The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. Weissenbach J.Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8). Tissue: Brain. |
| [7] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-956 AND 5133-6885, VARIANT MET-5186. Tissue: Spleen and Tongue. |
| [8] | "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3367-6885 (ISOFORM 2). Tissue: Brain. |
| [9] | "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION. |
| [10] | Ohara O., Nagase T., Kikuno R. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [11] | "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. Poustka A.Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5754-6885. |
| [12] | "Nuclear membrane proteins with potential disease links found by subtractive proteomics." Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L. Science 301:1380-1382(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. |
| [13] | "Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle." Zhang Q., Ragnauth C.D., Skepper J.N., Worth N.F., Warren D.T., Roberts R.G., Weissberg P.L., Ellis J.A., Shanahan C.M. J. Cell Sci. 118:673-687(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EMD AND LMNA. |
| [14] | "Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness." Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D. Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH SUN1 AND SUN2. |
| [15] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4108, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton." Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A., Gull K., Johnson C.A. J. Cell Sci. 122:2716-2726(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MKS3, FUNCTION. |
| [17] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4108, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [18] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-955, MASS SPECTROMETRY. |
| [19] | "Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes." Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S. J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUN1 AND SUN2. |
| [20] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2781 AND SER-6361, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [21] | "Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement." Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G. Science 329:956-959(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [22] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [23] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2781, MASS SPECTROMETRY. |
| [24] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-5940 AND CYS-6200. |
| [25] | "Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity." Zhang Q., Bethmann C., Worth N.F., Davies J.D., Wasner C., Feuer A., Ragnauth C.D., Yi Q., Mellad J.A., Warren D.T., Wheeler M.A., Ellis J.A., Skepper J.N., Vorgerd M., Schlotter-Weigel B., Weissberg P.L., Roberts R.G., Wehnert M., Shanahan C.M. Hum. Mol. Genet. 16:2816-2833(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EDMD5 MET-6211. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF435010 mRNA. Translation: AAL33547.1. AF435011 mRNA. Translation: AAL33548.1. AY061757 mRNA. Translation: AAL33800.1. AY061758 mRNA. Translation: AAL33801.1. AY061759 mRNA. Translation: AAL33802.1. AY184204 mRNA. Translation: AAO27772.1. AF495911 mRNA. Translation: AAN60443.1. AL117404 mRNA. Translation: CAB55905.2. Different initiation. AL162832 Genomic DNA. No translation available. AL355094 Genomic DNA. No translation available. AL359235 Genomic DNA. No translation available. BC042134 mRNA. Translation: AAH42134.1. BC071873 mRNA. Translation: AAH71873.1. AK074055 mRNA. Translation: BAB84881.1. Different initiation. AK090430 mRNA. Translation: BAC03411.1. AK095241 mRNA. Translation: BAC04506.1. AB023228 mRNA. Translation: BAA76855.3. AL080133 mRNA. Translation: CAB45729.1. Different initiation. | ||||||||||||||||||
| IPI | IPI00239405. IPI00239406. IPI00239409. IPI00239410. IPI00239413. IPI00239414. IPI00412276. IPI00815967. IPI01009561. | ||||||||||||||||||
| PIR | T12520. T17215. | ||||||||||||||||||
| RefSeq | NP_055995.4. NM_015180.4. NP_878914.1. NM_182910.2. NP_878917.1. NM_182913.2. NP_878918.2. NM_182914.2. | ||||||||||||||||||
| UniGene | Hs.525392. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | Q8WXH0. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | Q8WXH0. 5 interactions. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q8WXH0. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 116242809. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | Q8WXH0. | ||||||||||||||||||
| PRIDE | Q8WXH0. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000341472; ENSP00000344528; ENSG00000054654. ENST00000344113; ENSP00000341781; ENSG00000054654. ENST00000356081; ENSP00000348382; ENSG00000054654. ENST00000357395; ENSP00000349969; ENSG00000054654. ENST00000358025; ENSP00000350719; ENSG00000054654. ENST00000394768; ENSP00000378249; ENSG00000054654. ENST00000441438; ENSP00000396794; ENSG00000054654. ENST00000458046; ENSP00000391937; ENSG00000054654. ENST00000555002; ENSP00000450831; ENSG00000054654. ENST00000555022; ENSP00000451009; ENSG00000054654. | ||||||||||||||||||
| GeneID | 23224. | ||||||||||||||||||
| KEGG | hsa:23224. | ||||||||||||||||||
| UCSC | uc001xgk.3. human. uc001xgl.3. human. uc001xgm.3. human. uc001xgn.3. human. uc001xgs.3. human. uc001xgt.3. human. uc010aqa.3. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 23224. | ||||||||||||||||||
| GeneCards | GC14P064319. | ||||||||||||||||||
| HGNC | HGNC:17084. SYNE2. | ||||||||||||||||||
| HPA | HPA003435. | ||||||||||||||||||
| MIM | 608442. gene. 612999. phenotype. | ||||||||||||||||||
| neXtProt | NX_Q8WXH0. | ||||||||||||||||||
| Orphanet | 98853. Autosomal dominant Emery-Dreifuss muscular dystrophy. | ||||||||||||||||||
| PharmGKB | PA128394613. | ||||||||||||||||||
| HUGE | Search... | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG5069. | ||||||||||||||||||
| OMA | EDWHKFI. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Reactome | REACT_111183. Meiosis. REACT_115566. Cell Cycle. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q8WXH0. | ||||||||||||||||||
| Bgee | Q8WXH0. | ||||||||||||||||||
| Genevestigator | Q8WXH0. | ||||||||||||||||||
| GermOnline | ENSG00000054654. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 1.10.418.10. 2 hits. | ||||||||||||||||||
| InterPro | IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR012315. KASH. IPR018159. Spectrin/alpha-actinin. IPR002017. Spectrin_repeat. [Graphical view] | ||||||||||||||||||
| Pfam | PF00307. CH. 2 hits. PF10541. KASH. 1 hit. PF00435. Spectrin. 3 hits. [Graphical view] | ||||||||||||||||||
| SMART | SM00033. CH. 2 hits. SM00150. SPEC. 18 hits. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF47576. Calponin-homology. 1 hit. | ||||||||||||||||||
| PROSITE | PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS51049. KASH. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| GenomeRNAi | 23224. | ||||||||||||||||||
| NextBio | 44823. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | SYNE2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WXH0 Secondary accession number(s): Q540G1 Q9Y4R1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 14 Human chromosome 14: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
